메뉴 건너뛰기




Volumn 133, Issue 1-3, 2008, Pages 81-89

A new method for determining the constant-pressure heat capacity change associated with the protein denaturation induced by guanidinium chloride (or urea)

Author keywords

Heat capacity; Protein denaturation; Protein folding

Indexed keywords

AMINO ACID; GUANIDINE; UREA;

EID: 38949138456     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2007.12.006     Document Type: Article
Times cited : (12)

References (49)
  • 1
    • 0018588511 scopus 로고
    • Stability of proteins: small globular proteins
    • Privalov P.L. Stability of proteins: small globular proteins. Adv. Protein Chem. 33 (1979) 167-241
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 2
    • 0034141358 scopus 로고    scopus 로고
    • A possible origin of differences between calorimetric and equilibrium estimates of stability parameters of proteins
    • Sinha A., Yadav S., Ahmad R., and Ahmad F. A possible origin of differences between calorimetric and equilibrium estimates of stability parameters of proteins. Biochem. J. 345 (2000) 711-717
    • (2000) Biochem. J. , vol.345 , pp. 711-717
    • Sinha, A.1    Yadav, S.2    Ahmad, R.3    Ahmad, F.4
  • 3
    • 0034255443 scopus 로고    scopus 로고
    • A new method for the determination of stability parameters of proteins from their heat-induced denaturation curves
    • Yadav S., and Ahmad F. A new method for the determination of stability parameters of proteins from their heat-induced denaturation curves. Anal. Biochem. 283 (2000) 207-213
    • (2000) Anal. Biochem. , vol.283 , pp. 207-213
    • Yadav, S.1    Ahmad, F.2
  • 4
    • 0018782264 scopus 로고
    • The denaturation of ribonuclease-A by combinations of urea and salt denaturants
    • Ahmad F., and Bigelow C.C. The denaturation of ribonuclease-A by combinations of urea and salt denaturants. J. Mol. Biol. 131 (1979) 607-617
    • (1979) J. Mol. Biol. , vol.131 , pp. 607-617
    • Ahmad, F.1    Bigelow, C.C.2
  • 5
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford C. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24 (1970) 1-95
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 6
    • 0026709703 scopus 로고
    • Determining stability of proteins from guanidinium chloride transition curves
    • Ahmad F., Yadav S., and Taneja S. Determining stability of proteins from guanidinium chloride transition curves. Biochem. J. 257 (1992) 481-485
    • (1992) Biochem. J. , vol.257 , pp. 481-485
    • Ahmad, F.1    Yadav, S.2    Taneja, S.3
  • 7
    • 0017802519 scopus 로고
    • Solvent denaturation
    • Schellman J.A. Solvent denaturation. Biopolymers 17 (1978) 1305-1322
    • (1978) Biopolymers , vol.17 , pp. 1305-1322
    • Schellman, J.A.1
  • 8
    • 0014604482 scopus 로고
    • Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25 °C
    • Aune K.C., and Tanford C. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25 °C. Biochemistry 8 (1969) 4586-4590
    • (1969) Biochemistry , vol.8 , pp. 4586-4590
    • Aune, K.C.1    Tanford, C.2
  • 9
    • 0014955678 scopus 로고
    • Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. III. Dependence on temperature
    • Tanford C., and Aune K.C. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. III. Dependence on temperature. Biochemistry 9 (1970) 206-211
    • (1970) Biochemistry , vol.9 , pp. 206-211
    • Tanford, C.1    Aune, K.C.2
  • 10
    • 0042622660 scopus 로고    scopus 로고
    • Equilibrium studies of the effect of difference in sequence homology on the mechanism of denaturation of bovine and horse cytochrome-c
    • Moza B., Qureshi S.H., and Ahmad F. Equilibrium studies of the effect of difference in sequence homology on the mechanism of denaturation of bovine and horse cytochrome-c. Biochim. Biophys. Acta 1646 (2003) 49-56
    • (2003) Biochim. Biophys. Acta , vol.1646 , pp. 49-56
    • Moza, B.1    Qureshi, S.H.2    Ahmad, F.3
  • 11
    • 0024498471 scopus 로고
    • A new method for determining the heat-capacity change from protein folding
    • Pace C.N., and Laurent D.V. A new method for determining the heat-capacity change from protein folding. Biochemistry 28 (1989) 2520-2525
    • (1989) Biochemistry , vol.28 , pp. 2520-2525
    • Pace, C.N.1    Laurent, D.V.2
  • 13
    • 0030933329 scopus 로고    scopus 로고
    • Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility
    • Creamer T.P., Srinivasan R., and Rose G.D. Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility. Biochemistry 36 (1997) 2832-2835
    • (1997) Biochemistry , vol.36 , pp. 2832-2835
    • Creamer, T.P.1    Srinivasan, R.2    Rose, G.D.3
  • 14
    • 0000881274 scopus 로고
    • Structure of muramidase (lysozyme). I. The effect of guanidine hydrochloride on muramidase
    • Hamaguchi K., and Kurono A. Structure of muramidase (lysozyme). I. The effect of guanidine hydrochloride on muramidase. J. Biochem. (Tokyo) 54 (1963) 111-122
    • (1963) J. Biochem. (Tokyo) , vol.54 , pp. 111-122
    • Hamaguchi, K.1    Kurono, A.2
  • 15
    • 0038199771 scopus 로고
    • Difference spectra of ribonuclease and two ribonuclease derivatives
    • Bigelow C.C. Difference spectra of ribonuclease and two ribonuclease derivatives. C. R. Trav. Lab. Carlsberg. 31 (1960) 305-324
    • (1960) C. R. Trav. Lab. Carlsberg. , vol.31 , pp. 305-324
    • Bigelow, C.C.1
  • 16
    • 0015784343 scopus 로고
    • Equilibrium and kinetics of the unfolding of alpha-lactalbumin by guanidine hydrochloride
    • Sugai S., Yashiro H., and Nitta K. Equilibrium and kinetics of the unfolding of alpha-lactalbumin by guanidine hydrochloride. Biochim. Biophys. Acta 328 (1973) 35-41
    • (1973) Biochim. Biophys. Acta , vol.328 , pp. 35-41
    • Sugai, S.1    Yashiro, H.2    Nitta, K.3
  • 17
    • 0029156116 scopus 로고
    • Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding
    • Pace C.N. Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding. Methods Enzymol. 259 (1995) 538-554
    • (1995) Methods Enzymol. , vol.259 , pp. 538-554
    • Pace, C.N.1
  • 18
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-289
    • (1986) Methods Enzymol. , vol.131 , pp. 266-289
    • Pace, C.N.1
  • 19
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant J.M. Biochemical applications of differential scanning calorimetry. Annu. Rev. Phys. Chem. 38 (1987) 463-488
    • (1987) Annu. Rev. Phys. Chem. , vol.38 , pp. 463-488
    • Sturtevant, J.M.1
  • 20
    • 0020479709 scopus 로고
    • Estimation of the free energy of stabilization of ribonuclease A, lysozyme, alpha-lactalbumin, and myoglobin
    • Ahmad F., and Bigelow C.C. Estimation of the free energy of stabilization of ribonuclease A, lysozyme, alpha-lactalbumin, and myoglobin. J. Biol. Chem. 257 (1982) 12935-12938
    • (1982) J. Biol. Chem. , vol.257 , pp. 12935-12938
    • Ahmad, F.1    Bigelow, C.C.2
  • 21
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 23
    • 5944250450 scopus 로고
    • Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acids
    • Momany F.A., Mc Guire R.F., Burgess A.W., and Scheraga H.A. Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acids. J. Phys. Chem. 79 (1975) 2361-2381
    • (1975) J. Phys. Chem. , vol.79 , pp. 2361-2381
    • Momany, F.A.1    Mc Guire, R.F.2    Burgess, A.W.3    Scheraga, H.A.4
  • 24
    • 0027349239 scopus 로고
    • Hydration and heat stability effects on protein unfolding
    • Oobatake M., and Ooi T. Hydration and heat stability effects on protein unfolding. Prog. Biophys. Mol. Biol. 59 (1993) 237-284
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 237-284
    • Oobatake, M.1    Ooi, T.2
  • 25
    • 0037340834 scopus 로고    scopus 로고
    • Real value prediction of solvent accessibility from amino acid sequence
    • Ahmad S., Gromiha M.M., and Sarai A. Real value prediction of solvent accessibility from amino acid sequence. Proteins 50 (2003) 629-635
    • (2003) Proteins , vol.50 , pp. 629-635
    • Ahmad, S.1    Gromiha, M.M.2    Sarai, A.3
  • 26
    • 0026168401 scopus 로고
    • Protein stability from denaturation transition curves
    • Ahmad F. Protein stability from denaturation transition curves. Ind. J. Biochem. Biophys. 28 (1991) 168-173
    • (1991) Ind. J. Biochem. Biophys. , vol.28 , pp. 168-173
    • Ahmad, F.1
  • 27
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl a-chymotrypsin using different denaturants
    • Santoro M.M., and Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl a-chymotrypsin using different denaturants. Biochemistry 27 (1988) 8063-8068
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 28
    • 0028174361 scopus 로고
    • Energetics of the alpha-lactalbumin states: a calorimetric and statistical thermodynamic study
    • Griko Y.V., Freire E., and Privalov P.L. Energetics of the alpha-lactalbumin states: a calorimetric and statistical thermodynamic study. Biochemistry 33 (1994) 1889-1899
    • (1994) Biochemistry , vol.33 , pp. 1889-1899
    • Griko, Y.V.1    Freire, E.2    Privalov, P.L.3
  • 29
    • 0026315736 scopus 로고
    • Effect of reductive alkylation on thermal stability of ribonuclease A and chymotrypsinogen A
    • Fujita Y., and Noda Y. Effect of reductive alkylation on thermal stability of ribonuclease A and chymotrypsinogen A. Int. J. Pept. Protein Res. 38 (1991) 445-452
    • (1991) Int. J. Pept. Protein Res. , vol.38 , pp. 445-452
    • Fujita, Y.1    Noda, Y.2
  • 30
    • 0033596719 scopus 로고    scopus 로고
    • Protein Stability: Functional dependence of denaturational Gibbs energy on urea concentration
    • Gupta R., and Ahmad F. Protein Stability: Functional dependence of denaturational Gibbs energy on urea concentration. Biochemistry 38 (1999) 2471-2479
    • (1999) Biochemistry , vol.38 , pp. 2471-2479
    • Gupta, R.1    Ahmad, F.2
  • 31
    • 0018780588 scopus 로고
    • Thermodynamics of the denaturation of lysozyme in alcohol-water mixtures
    • Velicelebi G., and Sturtevant J.M. Thermodynamics of the denaturation of lysozyme in alcohol-water mixtures. Biochemistry 18 (1979) 1180-1186
    • (1979) Biochemistry , vol.18 , pp. 1180-1186
    • Velicelebi, G.1    Sturtevant, J.M.2
  • 32
    • 0031822735 scopus 로고    scopus 로고
    • Transition state in the folding of {alpha}-lactalbumin probed by the 6-120 disulfide bond
    • Ikeguchi M., Fujino M., Kato M., Kuwajima K., and Sugai S. Transition state in the folding of {alpha}-lactalbumin probed by the 6-120 disulfide bond. Protein Sci. 7 (1998) 1564-1574
    • (1998) Protein Sci. , vol.7 , pp. 1564-1574
    • Ikeguchi, M.1    Fujino, M.2    Kato, M.3    Kuwajima, K.4    Sugai, S.5
  • 33
    • 0014963345 scopus 로고
    • Thermodynamics of protein denaturation. A calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation
    • Jackson M., and Brandts J.F. Thermodynamics of protein denaturation. A calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation. Biochemistry 9 (1970) 2294-2301
    • (1970) Biochemistry , vol.9 , pp. 2294-2301
    • Jackson, M.1    Brandts, J.F.2
  • 34
    • 0029786885 scopus 로고    scopus 로고
    • Protein stability: urea-induced versus guanidine-induced unfolding of metmyoglobin
    • Gupta R., Yadav S., and Ahmad F. Protein stability: urea-induced versus guanidine-induced unfolding of metmyoglobin. Biochemistry 35 (1996) 11925-11930
    • (1996) Biochemistry , vol.35 , pp. 11925-11930
    • Gupta, R.1    Yadav, S.2    Ahmad, F.3
  • 35
    • 0027978242 scopus 로고
    • Increased thermal stability of proteins in the presence of amino acids
    • Taneja S., and Ahmad F. Increased thermal stability of proteins in the presence of amino acids. Biochem. J. 303 (1994) 147-153
    • (1994) Biochem. J. , vol.303 , pp. 147-153
    • Taneja, S.1    Ahmad, F.2
  • 36
    • 0030458930 scopus 로고    scopus 로고
    • A model-independent, nonlinear extrapolation procedure for the characterization of protein folding energetics from solvent-denaturation data
    • Ibarra-Molero B., and Sanchez-Ruiz J.M. A model-independent, nonlinear extrapolation procedure for the characterization of protein folding energetics from solvent-denaturation data. Biochemistry 35 (1996) 14689-14702
    • (1996) Biochemistry , vol.35 , pp. 14689-14702
    • Ibarra-Molero, B.1    Sanchez-Ruiz, J.M.2
  • 37
    • 0028960492 scopus 로고
    • How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease-A stability
    • Yao M., and Bolen D.W. How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease-A stability. Biochemistry 34 (1995) 3771-3781
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 38
    • 0008750928 scopus 로고
    • A scanning calorimetric study of bovine and human apo-a-lactalbumin
    • Pfeil W., and Sadowski M.L. A scanning calorimetric study of bovine and human apo-a-lactalbumin. Stud. Biophys. 109 (1985) 163-170
    • (1985) Stud. Biophys. , vol.109 , pp. 163-170
    • Pfeil, W.1    Sadowski, M.L.2
  • 39
    • 0343247668 scopus 로고    scopus 로고
    • The native and the heat-induced denatured states of alpha-chymotrypsinogen A: thermodynamic and spectroscopic studies
    • Chalikian T.V., Voelker J., Anafi D., and Breslauer K.J. The native and the heat-induced denatured states of alpha-chymotrypsinogen A: thermodynamic and spectroscopic studies. J. Mol. Biol. 274 (1997) 237-252
    • (1997) J. Mol. Biol. , vol.274 , pp. 237-252
    • Chalikian, T.V.1    Voelker, J.2    Anafi, D.3    Breslauer, K.J.4
  • 40
  • 41
    • 0016505899 scopus 로고
    • The stability of globular proteins
    • Pace C.N. The stability of globular proteins. CRC Crit. Rev. Biochem. 3 (1975) 1-43
    • (1975) CRC Crit. Rev. Biochem. , vol.3 , pp. 1-43
    • Pace, C.N.1
  • 42
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro M.M., and Bolen D.W. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry 31 (1992) 4901-4907
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 43
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidinium chloride. A calorimetric study
    • Makhatadze G.I., and Privalov P.L. Protein interactions with urea and guanidinium chloride. A calorimetric study. J. Mol. Biol. 226 (1992) 491-505
    • (1992) J. Mol. Biol. , vol.226 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 44
    • 0017878090 scopus 로고
    • Thermodynamics of the denaturation of pepsinogen by urea
    • Ahmad F., and McPhie P. Thermodynamics of the denaturation of pepsinogen by urea. Biochemistry 17 (1978) 241-246
    • (1978) Biochemistry , vol.17 , pp. 241-246
    • Ahmad, F.1    McPhie, P.2
  • 45
    • 0017166109 scopus 로고
    • Reversible unfolding of the major fraction of ovalbumin by guanidine hydrochloride
    • Ahmad F., and Salahuddin A. Reversible unfolding of the major fraction of ovalbumin by guanidine hydrochloride. Biochemistry 15 (1976) 5168-5175
    • (1976) Biochemistry , vol.15 , pp. 5168-5175
    • Ahmad, F.1    Salahuddin, A.2
  • 47
    • 0027640940 scopus 로고
    • Hydrophobicity and stability for a family of model proteins
    • Muller N. Hydrophobicity and stability for a family of model proteins. Biopolymers 33 (1993) 1185-1193
    • (1993) Biopolymers , vol.33 , pp. 1185-1193
    • Muller, N.1
  • 48
    • 0029843132 scopus 로고    scopus 로고
    • Hydrogen bonding stabilizes globular proteins
    • Myers J.K., and Pace C.N. Hydrogen bonding stabilizes globular proteins. Biophys. J. 71 (1996) 2033-2039
    • (1996) Biophys. J. , vol.71 , pp. 2033-2039
    • Myers, J.K.1    Pace, C.N.2
  • 49
    • 84996108580 scopus 로고
    • Estimation of the stability of globular proteins
    • Ahmad F., and Bigelow C.C. Estimation of the stability of globular proteins. Biopolymers 25 (1986) 1623-1633
    • (1986) Biopolymers , vol.25 , pp. 1623-1633
    • Ahmad, F.1    Bigelow, C.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.